GWL_AILME
ID GWL_AILME Reviewed; 882 AA.
AC D2HXI8;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Serine/threonine-protein kinase greatwall;
DE Short=GW;
DE Short=GWL;
DE EC=2.7.11.1;
DE AltName: Full=Microtubule-associated serine/threonine-protein kinase-like;
DE Short=MAST-L;
GN Name=MASTL; Synonyms=GW, GWL; ORFNames=PANDA_017354;
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
CC -!- FUNCTION: Serine/threonine kinase that plays a key role in M phase by
CC acting as a regulator of mitosis entry and maintenance. Acts by
CC promoting the inactivation of protein phosphatase 2A (PP2A) during M
CC phase: does not directly inhibit PP2A but acts by mediating
CC phosphorylation and subsequent activation of ARPP19 and ENSA at 'Ser-
CC 62' and 'Ser-67', respectively. ARPP19 and ENSA are phosphatase
CC inhibitors that specifically inhibit the PPP2R2D (PR55-delta) subunit
CC of PP2A. Inactivation of PP2A during M phase is essential to keep
CC cyclin-B1-CDK1 activity high. Following DNA damage, it is also involved
CC in checkpoint recovery by being inhibited (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000250}. Nucleus. Note=During interphase is
CC mainly nuclear, upon nuclear envelope breakdown localizes at the
CC cytoplasm and during mitosis at the centrosomes. {ECO:0000250}.
CC -!- PTM: Phosphorylation at Thr-744 by CDK1 during M phase activates its
CC kinase activity. Maximum phosphorylation occurs in prometaphase (By
CC similarity). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. AGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
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DR EMBL; GL193622; EFB17868.1; -; Genomic_DNA.
DR RefSeq; XP_002927571.1; XM_002927525.3.
DR AlphaFoldDB; D2HXI8; -.
DR SMR; D2HXI8; -.
DR STRING; 9646.ENSAMEP00000001970; -.
DR PRIDE; D2HXI8; -.
DR Ensembl; ENSAMET00000002049; ENSAMEP00000001970; ENSAMEG00000001855.
DR GeneID; 100464443; -.
DR KEGG; aml:100464443; -.
DR CTD; 84930; -.
DR eggNOG; KOG0606; Eukaryota.
DR HOGENOM; CLU_016048_0_0_1; -.
DR InParanoid; D2HXI8; -.
DR OrthoDB; 878671at2759; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; ISS:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0007147; P:female meiosis II; IEA:Ensembl.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0000278; P:mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISS:UniProtKB.
DR GO; GO:1904668; P:positive regulation of ubiquitin protein ligase activity; IEA:Ensembl.
DR GO; GO:0006468; P:protein phosphorylation; IEA:InterPro.
DR CDD; cd05610; STKc_MASTL; 1.
DR InterPro; IPR000961; AGC-kinase_C.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR037638; MASTL_STKc.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR Pfam; PF00069; Pkinase; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS51285; AGC_KINASE_CTER; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW Acetylation; ATP-binding; Cell cycle; Cell division; Cytoplasm;
KW Cytoskeleton; Kinase; Mitosis; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..882
FT /note="Serine/threonine-protein kinase greatwall"
FT /id="PRO_0000408313"
FT DOMAIN 35..838
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 839..882
FT /note="AGC-kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00618"
FT REGION 713..736
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 156
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 41..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 62
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 207
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 222
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 293
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 371
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 521
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 554
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 558
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 633
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 671
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 725
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 744
FT /note="Phosphothreonine; by CDK1"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
FT MOD_RES 881
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96GX5"
SQ SEQUENCE 882 AA; 97948 MW; 18340891EF9F5A19 CRC64;
MEPTAGSEKE SEGDTVTGEC VNRIPVPRPP SIEEFTIVKP ISRGAFGKVY LGQKGGKLYA
VKVVKKADMI NKNMTHQVQA ERDALALSKS PFIVHLYYSL QSANNVYLVM EYLIGGDVKS
LLHIYGYFDE EMAVKYISEV ALALDYLHRH GIIHRDLKPD NMLISNEGHI KLTDFGLSKV
TLNRDINMMD ILTTPSMAKP RQDYSRTPGQ VLSLISSLGF FTPVAEKNKD SANILSTHVS
ETSQLSQGLV CPMSVDHRDT TPYSSKLLNS CLETVAPNPG MPVKCLTSHL LQSRRRLATS
SASSQSHTFV SSVESECHSS PRWEKDCQES DHALGYTVMS WNIIEKPSCT DSRDAIETKG
FNKKDLELAL SPIHNSSTIP ETGRSCVNLA KKGFPGEVSW EARELDINNI HVATDTAQSG
FHQSDQWAVD SGDATEEHLG KRGFKRNFEL VDSSPCQNII QHKKNCIEHK PRNAMSDGYI
NQRTGLTTEV QDLKLSVCGG QQSDCANKEN MVNSFIDKPQ TPEKSPVPMI AKNLLCELDE
DCDKNNKRDL LSSSLLCSDD ERASKSICMD SDSSFPGISV MESSLERQSL DPDKSIKESS
FEESNIEDLL TVSPRWQENI LPKGDENPAV QDSSQKMLAP SSKVLKTLTL SKRNAVAFRS
FNSHINASNN SEPSKMSLTS LDGMDISCVY SGSYPMAITP NQKGTSYIPY QQTPNQVKSG
TPYRTPKSVR RGAAPVDDGR ILGTPDYLAP ELLLGRAHGP AVDWWALGVC LFEFLTGIPP
FNDETPQQVF QNILKRDIPW PEGEEKLSDN SQNAVEILLT IDNAKRAGMK ELKRHHLFSD
VDWENLQHQT MPFIPQPDDE TDTSYFEARN NAQHLTISGF SL
